Induction of metallothionein production by zinc in human mononuclear cells.
1. Low mol. wt proteins with high Cd-binding capacity were found to be induced by Zn in cultured monocytes and lymphocytes. 2. In T cell cultures one protein was found to be induced by 125 microM Zn for 6 days, while in monocytes and B enriched cells under these conditions two proteins were found, of which the one with higher mol. wt had similar electrophoretic mobility to the T cell protein on polyacrylamide gels. 3. Mol. wt criteria and crossreactivity towards anti-metallothionein (Mt) antibody identified these proteins to be Mts of about 23 and 27 kDa mol. wt. 4. Metal binding studies indicated that monocyte and lymphocyte Mts had a higher affinity to Zn compared to Cd than rat liver Mt and Mts from Cd-resistant substrains of a human epithelial and a murine fibroblast cell line. 5. The presence of the T cell mitogen phytohemagglutinin (PHA) was found not to be necessary for this Mt induction by Zn.
Mesna
O J
OJ
Department of Immunology, National Institute of Public Health, Norway.
Steffensen
I L
IL
Melhuus
A
A
Hjertholm
H
H
Heier
H E
HE
Andersen
R A
RA
D001402:B-Lymphocytes / Q000378:metabolism*; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008668:Metallothionein / Q000096:biosynthesis*; D008970:Molecular Weight; D009000:Monocytes / Q000378:metabolism*; D013601:T-Lymphocytes / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism / Q000494:pharmacology*
D008668:Metallothionein; D015032:Zinc